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dc.contributor.authorKoppikar, Anuradha Rajesh
dc.date.accessioned2014-03-04T03:26:54Z
dc.date.available2014-03-04T03:26:54Z
dc.date.issued2008-08
dc.identifier.otherkoppikar_anuradha_r_200808_ms
dc.identifier.urihttp://purl.galileo.usg.edu/uga_etd/koppikar_anuradha_r_200808_ms
dc.identifier.urihttp://hdl.handle.net/10724/24964
dc.description.abstractO-linked mannose has been implicated in cell-cell and cell-matrix adhesion. Defects in glycosyltransferases that add or extend O-linked mannose on glycoproteins generate neuron migration defects in congenital muscular dystrophies (CMD). The only well characterized O-mannose modified mammalian protein has been the peripheral membrane protein alpha-dystroglycan (±-DG). We propose that there must be other O-mannosylated proteins that modulate the CMD phenotype since O-mannosylation comprises a third of all O-linked glycans in the brain, and a brain ±-DG knockout does not recapitulate all neuronal aspects of CMD. This research proposal aims to develop a chemoenzymatic labeling method to identify those proteins. Elucidating the functional role of O-mannose would contribute towards existing knowledge of how extracellular glycosylation participates in a broad range of human disorders and tissue functions while also paving the way for glycopeptide and enzyme based therapeutics. KEYWORDS: O-Mannose, Neuron Migration, Chemoenzymatic Labeling USING CHEMOENZYMATIC LABELING TO PROBE O-MANNOSE GLYCOSYLATION By ANURADHA R. KOPPIKAR B.S., Georgia Institute of Technology, 2005 A Thesis Submitted to the Graduate Faculty of The University of Georgia in Partial Fulfillment of the Requirements for the Degree MASTER OF SCIENCE ATHENS, GA 2008
dc.languageeng
dc.publisheruga
dc.rightspublic
dc.subjectO-mannose
dc.subjectneuron migration
dc.subjectchemoenzymatic labeling
dc.titleUsing chemoenzymatic labeling to probe O-mannose glycosylation
dc.typeThesis
dc.description.degreeMS
dc.description.departmentBiochemistry and Molecular Biology
dc.description.majorBiochemistry and Molecular Biology
dc.description.advisorLance Wells
dc.description.committeeLance Wells
dc.description.committeeMichael Pierce
dc.description.committeeCarl Bergmann
dc.description.committeeMichael Tiemeyer


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